Citation
Mollica, Adriano, et al. "Exploring New Probenecid-based Carbonic Anhydrase Inhibitors: Synthesis, Biological Evaluation and Docking Studies." Bioorganic & Medicinal Chemistry, vol. 23, no. 17, 2015, pp. 5311-8.
Mollica A, Costante R, Akdemir A, et al. Exploring new Probenecid-based carbonic anhydrase inhibitors: Synthesis, biological evaluation and docking studies. Bioorg Med Chem. 2015;23(17):5311-8.
Mollica, A., Costante, R., Akdemir, A., Carradori, S., Stefanucci, A., Macedonio, G., Ceruso, M., & Supuran, C. T. (2015). Exploring new Probenecid-based carbonic anhydrase inhibitors: Synthesis, biological evaluation and docking studies. Bioorganic & Medicinal Chemistry, 23(17), 5311-8. https://doi.org/10.1016/j.bmc.2015.07.066
Mollica A, et al. Exploring New Probenecid-based Carbonic Anhydrase Inhibitors: Synthesis, Biological Evaluation and Docking Studies. Bioorg Med Chem. 2015 Sep 1;23(17):5311-8. PubMed PMID: 26264840.
TY - JOUR
T1 - Exploring new Probenecid-based carbonic anhydrase inhibitors: Synthesis, biological evaluation and docking studies.
AU - Mollica,Adriano,
AU - Costante,Roberto,
AU - Akdemir,Atilla,
AU - Carradori,Simone,
AU - Stefanucci,Azzurra,
AU - Macedonio,Giorgia,
AU - Ceruso,Mariangela,
AU - Supuran,Claudiu T,
Y1 - 2015/08/01/
PY - 2015/05/13/received
PY - 2015/07/28/revised
PY - 2015/07/29/accepted
PY - 2015/8/13/entrez
PY - 2015/8/13/pubmed
PY - 2016/5/27/medline
KW - Molecular modeling
KW - Probenecid
KW - Selective carbonic anhydrase IX inhibitors
KW - Selective carbonic anhydrase XII inhibitors
KW - Tertiary sulfonamides
SP - 5311
EP - 8
JF - Bioorganic & medicinal chemistry
JO - Bioorg Med Chem
VL - 23
IS - 17
N2 - Novel Probenecid-based amide derivatives, incorporating different natural amino acids, were synthesized and assayed to test their effect on the human carbonic anhydrase (hCA, EC 4.2.1.1) transmembrane isoforms hCA IX and XII over the ubiquitous isoforms hCA I and II. Most of them presented a complete loss of hCA II inhibition (K(i)s > 10,000 nM) and strong inhibitory activity against hCA IX and XII in the nanomolar range with respect to the parent compound. A residual activity against hCA I was observed for some of them. These biological results have been explained by docking studies within the active sites of the four studied human carbonic anhydrases (with or without the zinc-bound water) and helped us to better comprehend the rationale behind the design of tertiary sulfonamide compounds as potent but atypical inhibitors of specific isoforms of human carbonic anhydrase.
SN - 1464-3391
UR - https://www.unboundmedicine.com/medline/citation/26264840/Exploring_new_Probenecid_based_carbonic_anhydrase_inhibitors:_Synthesis_biological_evaluation_and_docking_studies_
L2 - https://linkinghub.elsevier.com/retrieve/pii/S0968-0896(15)00650-1
DB - PRIME
DP - Unbound Medicine
ER -